Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mass Spectrometric Characterization of Amyloid-β Species in the 7PA2 Cell Model of Alzheimer's Disease

3 Dec 2012

Abstract excerpt

The Chinese hamster ovary cell line 7PA2, stably transfected with the 751 amino acid isoform of amyloid-β protein precursor (AβPP) containing the Val → Phe mutation at residue 717, is one of the most used models to study the biochemistry and toxicity of secreted amyloid-β (Aβ) peptides, particularly Aβ oligomers, which are considered to be of relevance to the pathogenesis of Alzheimer's disease. Here, we present...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alzheimer's disease research and treatments
Share to Cholinesterase and Neurodegenerative Diseases
Share to Computational Drug Discovery Methods

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 22886024
DOI: 10.3233/jad-2012-120994

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 24 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mass Spectrometric Characterization of Amyloid-β Species in the 7PA2 Cell Model of Alzheimer's DiseasePMID 22886024Read ↗

Outstanding Phenotypic Differences in the Profile of Amyloid-β between Tg2576 and APPswe/PS1dE9 Transgenic Mouse Models of Alzheimer's Disease.Semantic proximity Read ↗

Understanding Aβ25-35 peptide altered exosomal proteome and associated pathways linked with the Alzheimer’s disease pathogenesis using human neuroblastoma SH-SY5Y CellsSemantic proximity Read ↗

Cells with a familial Alzheimer's disease mutation produce authentic beta-peptide.Semantic proximity Read ↗

Generation and regulation of beta-amyloid peptide variants by neurons.Semantic proximity Read ↗

Enhanced Production and Oligomerization of the 42-residue Amyloid β-Protein by Chinese Hamster Ovary Cells Stably Expressing Mutant PresenilinsSemantic proximity Read ↗

Emerging roles of N- and C-terminally truncated Aβ species in Alzheimer’s diseaseSemantic proximity Read ↗

Elevation of beta-amyloid peptide 2-42 in sporadic and familial Alzheimer's disease and its generation in PS1 knockout cells.Semantic proximity Read ↗

The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid beta protein ending at the 42nd (or 43rd) residue.Semantic proximity Read ↗

An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants.Semantic proximity Read ↗

Identification of NEEP21 as a β-Amyloid Precursor Protein-Interacting Protein<i>In Vivo</i>That Modulates Amyloidogenic Processing<i>In Vitro</i>Semantic proximity Read ↗

The aqueous phase of Alzheimer's disease brain contains assemblies built from ∼4 and ∼7 kDa Aβ speciesSemantic proximity Read ↗

Altered processing of a mutant amyloid precursor protein in neuronal and endothelial cells.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.